1gku
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(New page: 200px<br /><applet load="1gku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gku, resolution 2.7Å" /> '''REVERSE GYRASE FROM A...)
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Revision as of 14:00, 20 November 2007
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REVERSE GYRASE FROM ARCHAEOGLOBUS FULGIDUS
Overview
Reverse gyrase is the only topoisomerase known to positively supercoil, DNA. The protein appears to be unique to hyperthermophiles, where its, activity is believed to protect the genome from denaturation. The 120 kDa, enzyme is the only member of the type I topoisomerase family that requires, ATP, which is bound and hydrolysed by a helicase-like domain. We have, determined the crystal structure of reverse gyrase from Archaeoglobus, fulgidus in the presence and absence of nucleotide cofactor. The structure, provides the first view of an intact supercoiling enzyme, explains, mechanistic differences from other type I topoisomerases and suggests a, model for how the two domains of the protein cooperate to positively, supercoil DNA. Coordinates have been deposited in the Protein Data Bank, under accession codes 1GKU and 1GL9.
About this Structure
1GKU is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA., Rodriguez AC, Stock D, EMBO J. 2002 Feb 1;21(3):418-26. PMID:11823434
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